Proteolysis at a lysine residue abolishes the recetor-recognition site of α2-Macroglobulin complexes

FEBS Letters

Volumn 137, Issue 2, 1982, Pages 241-244

  Marynen, Peter ^a   Van Leuven, Fred ^a   Cassiman, Jean Jacques ^a   Van Den Berghe, Herman ^a  

^a UNIVERSITY OF LEUVEN   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 2 MACROGLOBULIN; IMMUNOGLOBULIN RECEPTOR; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; LYSINE;

ARTICLE; BINDING SITE; CELL CULTURE; FIBROBLAST; HUMAN; KINETICS; METABOLISM; SKIN;

ALPHA-MACROGLOBULINS; BINDING SITES; CELLS, CULTURED; FIBROBLASTS; HUMAN; KINETICS; LDL-RECEPTOR RELATED PROTEIN 1; LYSINE; RECEPTORS, IMMUNOLOGIC; SKIN; SUPPORT, NON-U.S. GOV'T;

EID: 0020490219     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/0014-5793(82)80358-X     Document Type: Article

References (19)

1. A monoclonal antibody to a neo-antigen on alpha 2-macroglobulin complexes inhibits receptor-mediated endocytosis.
2. Qualitative and quantitative study of the growth and cell surface properties of Huntington's disease fibroblasts and age-matched controls